ID   SH3B4_SERQU             Reviewed;         966 AA.
AC   Q8AXQ3; Q8JIP1; Q8JIQ1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 64.
DE   RecName: Full=SH3 domain-binding protein 4;
GN   Name=sh3bp4;
OS   Seriola quinqueradiata (Five-ray yellowtail).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Carangiformes; Carangidae; Seriola.
OX   NCBI_TaxID=8161;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Doi M., Abe S., Nakagawa T.;
RT   "Seriora quinqueradiata mRNA of SH3BP4.";
RL   Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Possible role in regulating endocytosis of the transferrin
CC       receptor at the plasma membrane. Alternatively, may function as a
CC       negative regulator of the amino acid-induced TOR signaling by
CC       inhibiting the formation of active Rag GTPase complexes. Preferentially
CC       binds inactive Rag GTPase complexes and prevents their interaction with
CC       the mTORC1 complex inhibiting its relocalization to lysosomes and its
CC       activation. Thereby, may indirectly regulate cell growth, proliferation
CC       and autophagy (By similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Homodimer or homooligomer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Membrane, clathrin-coated pit {ECO:0000250}.
CC       Cytoplasmic vesicle, clathrin-coated vesicle {ECO:0000250}. Nucleus
CC       {ECO:0000250}. Note=Specifically associated with transferrin receptor-
CC       containing clathrin-coated pits and clathrin-coated vesicles. May also
CC       localize to the nucleus (By similarity). {ECO:0000250}.
CC   -!- DOMAIN: The SH3 domain mediates localization to the clathrin-coated
CC       pits and vesicles. {ECO:0000250}.
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DR   EMBL; AB074980; BAB96751.1; -; mRNA.
DR   EMBL; AB077749; BAC02945.1; -; mRNA.
DR   EMBL; AB086184; BAC41718.1; -; mRNA.
DR   AlphaFoldDB; Q8AXQ3; -.
DR   SMR; Q8AXQ3; -.
DR   GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR   GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0071230; P:cellular response to amino acid stimulus; ISS:UniProtKB.
DR   GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISS:UniProtKB.
DR   GO; GO:0008285; P:negative regulation of cell population proliferation; ISS:UniProtKB.
DR   GO; GO:0034260; P:negative regulation of GTPase activity; ISS:UniProtKB.
DR   GO; GO:0032007; P:negative regulation of TOR signaling; ISS:UniProtKB.
DR   GO; GO:0010508; P:positive regulation of autophagy; ISS:UniProtKB.
DR   GO; GO:0061462; P:protein localization to lysosome; ISS:UniProtKB.
DR   GO; GO:0050790; P:regulation of catalytic activity; ISS:UniProtKB.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR035455; SH3BP4.
DR   InterPro; IPR000906; ZU5_dom.
DR   PANTHER; PTHR15603:SF3; PTHR15603:SF3; 1.
DR   Pfam; PF00018; SH3_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   Pfam; PF00791; ZU5; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF50044; SSF50044; 1.
DR   PROSITE; PS50002; SH3; 2.
DR   PROSITE; PS51145; ZU5; 1.
PE   2: Evidence at transcript level;
KW   Coated pit; Cytoplasmic vesicle; Endocytosis; Membrane; Nucleus; Repeat;
KW   SH3 domain.
FT   CHAIN           1..966
FT                   /note="SH3 domain-binding protein 4"
FT                   /id="PRO_0000274578"
FT   DOMAIN          57..116
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          322..457
FT                   /note="ZU5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00485"
FT   DOMAIN          657..727
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   CONFLICT        917
FT                   /note="I -> V (in Ref. 1; BAB96751)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   966 AA;  107179 MW;  34FF4EB8172B2B9E CRC64;
     MAAHRIRATT NNNTSLPRCK SEGTLIDLSE GVSEASLTDV KVPSPSALRL DATASFGAAR
     EVVAIKDCCP SSFTTLKFSK GDRLYVLDSS GAEWWYAHNN TEMGYIPAAY VEPINYRDSS
     FSDSGMIDTV GDCNEEAAKE MDLLGEWAGV ILKPTTFQNG NPFAATNSST NPFLNGGPQS
     PLDQNSNEKS VDLLLFDTLA PSVPNSTSIT ADINGFGSGV LNMNPLSPTV GVGQTLRRDN
     PFFRSKRSYS LSELSILQAQ SDAPQASTGF FGGLKAPAPE QFQSREDFRT AWLTHRKLAR
     SCHDLDSLGQ NPGWGQTQPV ETNIVCRLDS SGGAVQLPDA NISIHIPEGH VAPGDTQQIS
     IKALLDPPLE LNNDRCTTVS PVVEIKLSNM EIRTTVTLEM KVSVVVKIES RQTTEILCVR
     SDCKEGPYTP IPQAYIYGDM VQVCLDNLEP CMYVCVVAQS KSIAPDSTVW EHVVKKITLG
     VYGPKHIHPS FKTVVAMFGH DCAPKTLLVS EVGKQAQAVP PVALQLWGKH QFVLSRPQDL
     RVGVYSNMAN YEVKASEQAR VVRGFQVKLG KVSRLVYVIA SRNADDVSDF TLRIQIKDDQ
     DCILAQFCVQ TPTPPPKAGP KTSVQRRFLK KKEVGKIVLS PLAITTKYPV FQDRRINNLK
     FGKLIKTVIR QTKNQYLLEY KKGDFVALLS EEKIRLKGQL WTKEWYIGYY QGRLGFVHAK
     NVLVVGKVKP IYFSGPDLTT SLFLEQILKP CKFLTYIYAS VRTILMENIG NWRAFADSLG
     YINLPLTHFC RAELDSEPER VASVLEKLKE DCNNTESKER KSFQKELLTA LLKMDCQGLV
     ARLVMDFVLL TTAVELAGRW RELAEKLAKV SRQQMDAYEA PHRDKSGVVD SEAMWKPAYD
     FLVTWAAQIG DSYRDVIQEL HMGLDKMKNP ITKRWKHLTG TLILVNCMDA LRSSAFSPAA
     QDDCAI